2021
Limitation of phosphate assimilation maintains cytoplasmic magnesium homeostasis
Bruna RE, Kendra CG, Groisman EA, Pontes MH. Limitation of phosphate assimilation maintains cytoplasmic magnesium homeostasis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2021, 118: e2021370118. PMID: 33707210, PMCID: PMC7980370, DOI: 10.1073/pnas.2021370118.Peer-Reviewed Original ResearchConceptsCytoplasmic MgPhosphate assimilationRibosomal RNARegulatory logicP assimilationMolecular basisLoss of viabilityProtein inhibitsPi toxicityAdenosine triphosphateATP synthesisProtein synthesisATP accumulationHomeostasisBacterial growthCytosolic PiDependent processesMagnesium homeostasisBacteriaBiological moleculesInorganic orthophosphateEssential componentAssimilationGrowthRNA
1999
The Doa4 Deubiquitinating Enzyme Is Required for Ubiquitin Homeostasis in Yeast
Swaminathan S, Amerik A, Hochstrasser M. The Doa4 Deubiquitinating Enzyme Is Required for Ubiquitin Homeostasis in Yeast. Molecular Biology Of The Cell 1999, 10: 2583-2594. PMID: 10436014, PMCID: PMC25490, DOI: 10.1091/mbc.10.8.2583.Peer-Reviewed Original ResearchMeSH KeywordsCarrier ProteinsCytoskeletal ProteinsEndopeptidasesEndosomal Sorting Complexes Required for TransportFungal ProteinsHomeostasisMutationPeptide HydrolasesProteasome Endopeptidase ComplexSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin ThiolesteraseUbiquitinsVacuolesVesicular Transport ProteinsConceptsDeubiquitinating enzymeAttachment of ubiquitinUbiquitin-dependent proteolysisYeast Saccharomyces cerevisiaeWild-type cellsCell surface proteinsAdditional ubiquitinVacuolar proteolysisUbiquitinated substratesUbiquitin homeostasisCellular proteinsMembrane proteinsUbiquitinated intermediatesSaccharomyces cerevisiaeGenetic dataDoa4Loss of viabilityUbiquitin depletionUbiquitinProteolytic intermediatesProteasomeSurface proteinsUbiquitin degradationEventual degradationProtein
1996
The antibacterial action of protamine: evidence for disruption of cytoplasmic membrane energization in Salmonella typhimurium
Aspedon A, Groisman EA. The antibacterial action of protamine: evidence for disruption of cytoplasmic membrane energization in Salmonella typhimurium. Microbiology 1996, 142: 3389-3397. PMID: 9004502, DOI: 10.1099/13500872-142-12-3389.Peer-Reviewed Original ResearchConceptsCytoplasmic membraneNuclei of spermNutrient uptake functionsCellular ATP contentElectrical membrane potentialHigher delta psi valuesRespiring cellsLoss of viabilityMembrane energizationDifferent animal speciesProline uptakeProtein synthesisEnergy transductionMode of actionAnimal speciesUptake functionDelta psi valuesMembrane potentialCell lysisRapid effluxMechanism of actionPolycationic peptidesATP contentProtamineSalmonella typhimurium
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